Summary: Outer membrane protein OpcA
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This is the Wikipedia entry entitled "Outer membrane protein OpcA". More...
Outer membrane protein OpcA Edit Wikipedia article
| Outer membrane protein OpcA | |||||||||
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| Identifiers | |||||||||
| Symbol | OpcA | ||||||||
| Pfam | PF07239 | ||||||||
| InterPro | IPR009876 | ||||||||
| SCOP | 1k24 | ||||||||
| SUPERFAMILY | 1k24 | ||||||||
| OPM superfamily | 271 | ||||||||
| OPM protein | 1k24 | ||||||||
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Outer membrane adhesin OpcA protein family consists of several Neisseria species specific outer membrane proteins. Neisseria meningitidis causes meningococcal meningitis and septicemia. Opc (formerly called 5C) is one of the major outer membrane proteins and has been shown to play an important role in meningococcal adhesion and invasion of epithelial and endothelial cells, mediating attachment to host cells by binding proteoglycan cell-surface receptors.[1]
OpcA forms a 10-stranded beta-barrel with five highly mobile extracellular loops that protrude above the surface of the membrane.[2] These extracellular loops combine to form a crevice in the external surface that is lined by positively charged residues, which is predicted to be a binding site for proteoglycan polysaccharides involved in pathogenesis. Conformational changes in the extracellular loops modulate the surface of OpcA, which could affect the proteoglycan binding site.[3] These conformational changes could also lead to pore opening.
[edit] References
- ^ Zhu P, Klutch MJ, Derrick JP, Prince SM, Tsang RS, Tsai CM (2003). "Identification of opcA gene in Neisseria polysaccharea: interspecies diversity of Opc protein family". Gene 307: 31–40. doi:10.1016/S0378-1119(02)01208-8. PMID 12706886.
- ^ Derrick JP, Prince SM, Achtman M (2002). "Crystal structure of the OpcA integral membrane adhesin from Neisseria meningitidis". Proc. Natl. Acad. Sci. U.S.A. 99 (6): 3417–21. doi:10.1073/pnas.062630899. PMC 122538. PMID 11891340. //www.ncbi.nlm.nih.gov/pmc/articles/PMC122538/.
- ^ Sansom MS, Derrick JP, Bond PJ (2007). "Membrane Simulations of OpcA: Gating in the Loops?". Biophys. J. 92 (2): L23–5. doi:10.1529/biophysj.106.097311. PMC 1751375. PMID 17114231. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1751375/.
This article incorporates text from the public domain Pfam and InterPro IPR009876
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Outer membrane protein OpcA Provide feedback
This family consists of several Neisseria species specific OpcA outer membrane proteins. Opc (formerly called 5C) is one of the major outer membrane proteins and has been shown to play an important role in meningococcal adhesion and invasion of both epithelial and endothelial cells [1].
Literature references
-
Zhu P, Klutch MJ, Derrick JP, Prince SM, Tsang RS, Tsai CM; , Gene 2003;307:31-40.: Identification of opcA gene in Neisseria polysaccharea: interspecies diversity of Opc protein family. PUBMED:12706886 EPMC:12706886
External database links
| PANDIT: | PF07239 |
| Pseudofam: | PF07239 |
| SCOP: | 1k24 |
| SYSTERS: | OpcA |
This tab holds annotation information from the InterPro database.
InterPro entry IPR009876
This entry represents several Neisseria species-specific OpcA-type outer membrane adhesion proteins. OpcA (formerly called 5C) was isolated from Neisseria meningitidis, causative agent of meningococcal meningitis and septicemia. An outer membrane protein embedded in the lipid bilayer, OpcA was shown to play an important role in meningococcal adhesion and invasion of both epithelial and endothelial cells, mediating attachment to host cells by binding proteoglycan cell-surface receptors [PUBMED:12706886]. OpcA forms a 10-stranded beta-barrel with five highly mobile extracellular loops that protrude above the surface of the membrane [PUBMED:11891340]. These extracellular loops combine to form a crevice in the external surface that is lined by positively charged residues, which is predicted to be a binding site for proteoglycan polysaccharides involved in pathogenesis. Conformational changes in the extracellular loops modulate the surface of OpcA, which could affect the proteoglycan binding site [PUBMED:17114231]. These conformational changes could also lead to pore opening.
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan MBB (CL0193), which contains the following 54 members:
Ail_Lom Autotransporter Bac_surface_Ag Campylo_MOMP Channel_Tsx CopB DUF1302 DUF1597 DUF2320 DUF2490 DUF2860 DUF3078 DUF3138 DUF3187 DUF3308 DUF3374 DUF3575 DUF4289 DUF481 DUF560 Gcw_chp HP_OMP HP_OMP_2 KdgM LamB Legionella_OMP MipA OMP_b-brl OMP_b-brl_2 OMP_b-brl_3 OmpA_membrane Omptin OmpW Opacity OpcA OprB OprD OprF OstA_C PagL Phenol_MetA_deg Porin_1 Porin_2 Porin_4 Porin_O_P Porin_OmpG ShlB Surface_Ag_2 Toluene_X TonB_dep_Rec TraF_2 TSA Usher YfaZAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (2) |
Full (56) |
Representative proteomes | NCBI (42) |
Meta (0) |
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| RP15 (1) |
RP35 (1) |
RP55 (1) |
RP75 (2) |
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| Jalview | ||||||||
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| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (2) |
Full (56) |
Representative proteomes | NCBI (42) |
Meta (0) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (1) |
RP35 (1) |
RP55 (1) |
RP75 (2) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_17433 (release 10.0) |
| Previous IDs: | none |
| Type: | Family |
| Author: | Moxon SJ |
| Number in seed: | 2 |
| Number in full: | 56 |
| Average length of the domain: | 202.30 aa |
| Average identity of full alignment: | 53 % |
| Average coverage of the sequence by the domain: | 89.45 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 244 | ||||||||||||
| Family (HMM) version: | 6 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the OpcA domain has been found. There are 2 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence